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Showing 1-17 of 17 results for "C2643" within Papers
S B delCardayre et al.
The Journal of biological chemistry, 273(10), 5744-5751 (1998-04-16)
The human pathogen Staphylococcus aureus does not utilize the glutathione thiol/disulfide redox system employed by eukaryotes and many bacteria. Instead, this organism produces CoA as its major low molecular weight thiol. We report the identification and purification of the disulfide
Julie A Boylan et al.
Molecular microbiology, 59(2), 475-486 (2006-01-05)
The cellular responses of Borrelia burgdorferiTo reactive oxygen species (ROS) encountered during the different stages of its infective cycle are poorly understood. Few enzymes responsible for protecting proteins, DNA/RNA and lipids from damage by ROS have been identified and characterized.
V M Avakumov et al.
Eksperimental'naia i klinicheskaia farmakologiia, 56(1), 42-44 (1993-01-01)
Coenzyme A disulfide (CoA disulfide) was pharmacologically studied. It has been found to normalize lipid and carbohydrate metabolism when given in a dose of 2 mg/kg, i.m., in diverse liver dysfunctions. It possesses an antihypoxic action under hemic and histotoxic
H F Gilbert et al.
The Journal of biological chemistry, 256(4), 1782-1785 (1981-02-25)
The time-dependent inactivation of hydroxymethylglutaryl-CoA reductase from yeast by solutions of hydroxymethylglutaryl-CoA and CoASH is due to the rapid inactivation of the enzyme by oxidized CoA (CoA disulfide) present at trace levels in solutions of hydroxymethylglutaryl-CoA and CoASH. Solutions of
Rob Ofman et al.
The Biochemical journal, 393(Pt 2), 537-543 (2005-09-28)
Proteomic analysis of mouse kidney peroxisomes resulted in the identification of a novel nudix hydrolase designated RP2p, which is encoded by the D7RP2e gene. RP2p consists of 357 amino acids and contains two conserved domains: a nudix hydrolase domain and
Charles S Hummel et al.
FEMS microbiology letters, 252(2), 229-234 (2005-10-11)
Physiologically significant levels of intracellular coenzyme A were identified in Pyrococcus furiosus, Thermococcus litoralis, and Sulfolobus solfataricus, suggesting a role for CoA as an important low molecular mass thiol in the thermophilic Archaea. In P. furiosus, cells grown in the
L Gasmi et al.
The Biochemical journal, 357(Pt 1), 33-38 (2001-06-21)
A mouse homologue of the Saccharomyces cerevisiae Pcd1p coenzyme A diphosphatase, NUDT7alpha, has been expressed as a thioredoxin fusion protein in Escherichia coli. NUDT7alpha is also a CoA diphosphatase of the nudix hydrolase family, and hydrolyses CoA, CoA esters and
Farhad Forouhar et al.
The Journal of biological chemistry, 280(48), 40328-40336 (2005-10-08)
Bacillus subtilis PaiA has been implicated in the negative control of sporulation as well as production of degradative enzymes. PaiA shares recognizable sequence homology with N-acetyltransferases, including those that can acetylate spermidine/spermine substrates. We have determined the crystal structure of
Jamie R Wallen et al.
Biochemistry, 47(18), 5182-5193 (2008-04-11)
We have recently reported that CoASH is the major low-molecular weight thiol in Bacillus anthracis [Nicely, N. I. , Parsonage, D., Paige, C., Newton, G. L., Fahey, R. C., Leonardi, R., Jackowski, S., Mallett, T. C., and Claiborne, A. (2007)
J Luba et al.
Biochemistry, 38(9), 2725-2737 (1999-03-03)
An unusual flavoprotein disulfide reductase, which catalyzes the NADPH-dependent reduction of CoASSCoA, has recently been purified from the human pathogen Staphylococcus aureus [delCardayré, S. B., Stock, K. P., Newton, G. L., Fahey, R. C., and Davies, J. E. (1998) J.
Ivan Gout
Biochemical Society transactions, 47(1), 469-476 (2019-02-21)
Coenzyme A (CoA) is an indispensable cofactor in all living organisms. It is synthesized in an evolutionarily conserved pathway by enzymatic conjugation of cysteine, pantothenate (Vitamin B5), and ATP. This unique chemical structure allows CoA to employ its highly reactive
Roberta Leonardi et al.
Progress in lipid research, 44(2-3), 125-153 (2005-05-17)
Coenzyme A (CoA) is a ubiquitous essential cofactor that plays a central role in the metabolism of carboxylic acids, including short- and long-chain fatty acids. In the last few years, all of the genes encoding the CoA biosynthetic enzymes have
Hui Peng et al.
mSphere, 2(3) (2017-06-29)
Staphylococcus aureus is a commensal human pathogen and a major cause of nosocomial infections. As gaseous signaling molecules, endogenous hydrogen sulfide (H2S) and nitric oxide (NO·) protect S. aureus from antibiotic stress synergistically, which we propose involves the intermediacy of nitroxyl
T Conn Mallett et al.
Biochemistry, 45(38), 11278-11289 (2006-09-20)
Coenzyme A (CoASH) replaces glutathione as the major low molecular weight thiol in Staphylococcus aureus; it is maintained in the reduced state by coenzyme A-disulfide reductase (CoADR), a homodimeric enzyme similar to NADH peroxidase but containing a novel Cys43-SSCoA redox
Kevin D Revell et al.
Bioorganic & medicinal chemistry, 15(6), 2453-2467 (2007-01-30)
This study focuses on the mechanism of action of N-alkylthio beta-lactams, a new family of antibacterial compounds that show promising activity against Staphylococcus and Bacillus microbes. Previous investigations have determined that these compounds are highly selective towards these bacteria, and
S B delCardayre et al.
The Journal of biological chemistry, 273(10), 5752-5757 (1998-04-16)
The cdr gene encoding coenzyme A disulfide reductase (CoADR) from Staphylococcus aureus 8325-4 was cloned, sequenced, and overexpressed. The gene encodes a 438-amino acid polypeptide that has a calculated molecular weight of 49,200 and sequence similarity to the pyridine nucleotide-disulfide
Dennis R Harris et al.
The FEBS journal, 272(5), 1189-1200 (2005-02-22)
We have cloned NADH oxidase homologues from Pyrococcus horikoshii and P. furiosus, and purified the recombinant form of the P. horikoshii enzyme to homogeneity from Escherichia coli. Both enzymes (previously referred to as NOX2) have been shown to act as
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